| Year |
Citation |
Score |
| 2022 |
Biebl MM, Buchner J. p23 and Aha1: Distinct Functions Promote Client Maturation. Sub-Cellular Biochemistry. 101: 159-187. PMID 36520307 DOI: 10.1007/978-3-031-14740-1_6 |
0.332 |
|
| 2022 |
Strauch A, Rossa B, Köhler F, Haeussler S, Mühlhofer M, Rührnößl F, Körösy C, Bushman Y, Conradt B, Haslbeck M, Weinkauf S, Buchner J. The permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions. The Journal of Biological Chemistry. 102753. PMID 36442512 DOI: 10.1016/j.jbc.2022.102753 |
0.397 |
|
| 2022 |
Drwesh L, Heim B, Graf M, Kehr L, Hansen-Palmus L, Franz-Wachtel M, Macek B, Kalbacher H, Buchner J, Rapaport D. A network of cytosolic (co)chaperones promotes the biogenesis of mitochondrial signal-anchored outer membrane proteins. Elife. 11. PMID 35876647 DOI: 10.7554/eLife.77706 |
0.306 |
|
| 2022 |
Moessmer P, Suren T, Majdic U, Dahiya V, Rutz D, Buchner J, Rief M. Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments. Proceedings of the National Academy of Sciences of the United States of America. 119: e2119076119. PMID 35377810 DOI: 10.1073/pnas.2119076119 |
0.384 |
|
| 2022 |
Dahiya V, Rutz DA, Moessmer P, Mühlhofer M, Lawatscheck J, Rief M, Buchner J. The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones. Molecular Cell. PMID 35176233 DOI: 10.1016/j.molcel.2022.01.016 |
0.341 |
|
| 2021 |
Mühlhofer M, Peters C, Kriehuber T, Kreuzeder M, Kazman P, Rodina N, Reif B, Haslbeck M, Weinkauf S, Buchner J. Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble. Nature Communications. 12: 6697. PMID 34795272 DOI: 10.1038/s41467-021-27036-7 |
0.371 |
|
| 2021 |
Heider M, Eichner R, Stroh J, Morath V, Kuisl A, Zecha J, Lawatscheck J, Baek K, Garz AK, Rudelius M, Deuschle FC, Keller U, Lemeer S, Verbeek M, Götze KS, ... ... Buchner J, et al. The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma. Molecular Cell. PMID 33571422 DOI: 10.1016/j.molcel.2020.12.046 |
0.344 |
|
| 2021 |
Biebl MM, Lopez A, Rehn A, Freiburger L, Lawatscheck J, Blank B, Sattler M, Buchner J. Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle. Nature Communications. 12: 828. PMID 33547294 DOI: 10.1038/s41467-021-21063-0 |
0.364 |
|
| 2021 |
Noji M, Samejima T, Yamaguchi K, So M, Yuzu K, Chatani E, Akazawa-Ogawa Y, Hagihara Y, Kawata Y, Ikenaka K, Mochizuki H, Kardos J, Otzen DE, Bellotti V, Buchner J, et al. Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology. 4: 120. PMID 33500517 DOI: 10.1038/s42003-020-01641-6 |
0.34 |
|
| 2020 |
Biebl MM, Riedl M, Buchner J. Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation. Cell Reports. 32: 108063. PMID 32846121 DOI: 10.1016/J.Celrep.2020.108063 |
0.418 |
|
| 2020 |
Haslbeck M, Braun N, Stromer T, Richter B, Model N, Weinkauf S, Buchner J. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. The Embo Journal. 39: e105112. PMID 32548883 DOI: 10.15252/embj.2020105112 |
0.45 |
|
| 2020 |
Mader SL, Lopez A, Lawatscheck J, Luo Q, Rutz DA, Gamiz-Hernandez AP, Sattler M, Buchner J, Kaila VRI. Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90. Nature Communications. 11: 1410. PMID 32179743 DOI: 10.1038/S41467-020-15050-0 |
0.446 |
|
| 2020 |
Kazman P, Vielberg MT, Pulido Cendales MD, Hunziger L, Weber B, Hegenbart U, Zacharias M, Köhler R, Schönland S, Groll M, Buchner J. Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation. Elife. 9. PMID 32151314 DOI: 10.7554/Elife.52300 |
0.319 |
|
| 2020 |
Rehn A, Lawatscheck J, Jokisch ML, Mader SL, Luo Q, Tippel F, Blank B, Richter K, Lang K, Kaila VRI, Buchner J. A methylated lysine is a switch point for conformational communication in the chaperone Hsp90. Nature Communications. 11: 1219. PMID 32139682 DOI: 10.1038/S41467-020-15048-8 |
0.403 |
|
| 2019 |
Mühlhofer M, Berchtold E, Stratil CG, Csaba G, Kunold E, Bach NC, Sieber SA, Haslbeck M, Zimmer R, Buchner J. The Heat Shock Response in Yeast Maintains Protein Homeostasis by Chaperoning and Replenishing Proteins. Cell Reports. 29: 4593-4607.e8. PMID 31875563 DOI: 10.1016/J.Celrep.2019.11.109 |
0.325 |
|
| 2019 |
Weber B, Maier A, Buchner J. Peptides in proteins. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3235. PMID 31867828 DOI: 10.1002/Psc.3235 |
0.4 |
|
| 2019 |
Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S. The structure and oxidation of the eye lens chaperone αA-crystallin. Nature Structural & Molecular Biology. PMID 31792453 DOI: 10.1038/S41594-019-0332-9 |
0.427 |
|
| 2019 |
Mymrikov EV, Riedl M, Peters C, Weinkauf S, Haslbeck M, Buchner J. Regulation of small heat shock proteins by hetero-oligomer formation. The Journal of Biological Chemistry. PMID 31767683 DOI: 10.1074/Jbc.Ra119.011143 |
0.487 |
|
| 2019 |
Girstmair H, Tippel F, Lopez A, Tych K, Stein F, Haberkant P, Schmid PWN, Helm D, Rief M, Sattler M, Buchner J. The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range. Nature Communications. 10: 3626. PMID 31399574 DOI: 10.1038/S41467-019-11518-W |
0.464 |
|
| 2019 |
Boczek EE, Luo Q, Dehling M, Röpke M, Mader SL, Seidl A, Kaila VRI, Buchner J. Auto-phosphorylation activates c-Src kinase through global structural rearrangements. The Journal of Biological Chemistry. PMID 31331936 DOI: 10.1074/Jbc.Ra119.008199 |
0.334 |
|
| 2019 |
Dahiya V, Agam G, Lawatscheck J, Rutz DA, Lamb DC, Buchner J. Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries. Molecular Cell. PMID 31027879 DOI: 10.1016/J.Molcel.2019.03.026 |
0.413 |
|
| 2019 |
Schopf FH, Huber EM, Dodt C, Lopez A, Biebl MM, Rutz DA, Mühlhofer M, Richter G, Madl T, Sattler M, Groll M, Buchner J. The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2. Molecular Cell. PMID 30876805 DOI: 10.1016/J.Molcel.2019.02.011 |
0.462 |
|
| 2019 |
Carra S, Alberti S, Benesch JLP, Boelens W, Buchner J, Carver JA, Cecconi C, Ecroyd H, Gusev N, Hightower LE, Klevit RE, Lee HO, Liberek K, Lockwood B, Poletti A, et al. Small heat shock proteins: multifaceted proteins with important implications for life. Cell Stress & Chaperones. PMID 30758704 DOI: 10.1007/S12192-019-00979-Z |
0.417 |
|
| 2019 |
Biebl MM, Buchner J. Structure, Function, and Regulation of the Hsp90 Machinery. Cold Spring Harbor Perspectives in Biology. PMID 30745292 DOI: 10.1101/Cshperspect.A034017 |
0.44 |
|
| 2019 |
Dahiya V, Buchner J. Functional principles and regulation of molecular chaperones. Advances in Protein Chemistry and Structural Biology. 114: 1-60. PMID 30635079 DOI: 10.1016/Bs.Apcsb.2018.10.001 |
0.473 |
|
| 2019 |
Buchner J. Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series. The Journal of Biological Chemistry. PMID 30626733 DOI: 10.1074/Jbc.Rev118.006739 |
0.419 |
|
| 2019 |
Stavropoulou M, Asami S, Kaiser C, Haslbeck M, Buchner J, Weinkauf S, Reif B. Solution-state NMR assignment of the flexible C-terminal domain of the human eye lens molecular chaperone alphaA-crystallin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27109 |
0.334 |
|
| 2018 |
Weber B, Hora M, Kazman P, Göbl C, Camilloni C, Reif B, Buchner J. The Antibody Light-Chain Linker Regulates Domain Orientation and Amyloidogenicity. Journal of Molecular Biology. PMID 30414962 DOI: 10.1016/J.Jmb.2018.10.024 |
0.43 |
|
| 2018 |
Haslbeck M, Weinkauf S, Buchner J. Small heat shock proteins: Simplicity meets complexity. The Journal of Biological Chemistry. PMID 30385502 DOI: 10.1074/Jbc.Rev118.002809 |
0.479 |
|
| 2018 |
Suren T, Rutz D, Mößmer P, Merkel U, Buchner J, Rief M. Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor. Proceedings of the National Academy of Sciences of the United States of America. PMID 30366952 DOI: 10.1073/Pnas.1807618115 |
0.386 |
|
| 2018 |
Weber B, Brandl MJ, Pulido Cendales MD, Berner C, Pradhan T, Feind GM, Zacharias M, Reif B, Buchner J. A single residue switch reveals principles of antibody domain integrity. The Journal of Biological Chemistry. PMID 30228183 DOI: 10.1074/Jbc.Ra118.005475 |
0.406 |
|
| 2018 |
Tych KM, Jahn M, Gegenfurtner F, Hechtl VK, Buchner J, Hugel T, Rief M. Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90. The Journal of Physical Chemistry. B. PMID 30179494 DOI: 10.1021/Acs.Jpcb.8B07301 |
0.429 |
|
| 2018 |
Jores T, Lawatscheck J, Beke V, Franz-Wachtel M, Yunoki K, Fitzgerald JC, Macek B, Endo T, Kalbacher H, Buchner J, Rapaport D. Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins. The Journal of Cell Biology. PMID 29930205 DOI: 10.1083/Jcb.201712029 |
0.377 |
|
| 2018 |
Sabbagh JJ, Cordova RA, Zheng D, Criado-Marrero M, Lemus A, Li P, Baker JD, Nordhues BA, Darling AL, Martinez-Licha C, Rutz DA, Patel S, Buchner J, Leahy JW, Koren J, et al. Targeting the FKBP51/GR/Hsp90 complex to identify functionally relevant treatments for depression and PTSD. Acs Chemical Biology. PMID 29893552 DOI: 10.1021/Acschembio.8B00454 |
0.349 |
|
| 2018 |
Rutz DA, Luo Q, Freiburger L, Madl T, Kaila VRI, Sattler M, Buchner J. A switch point in the molecular chaperone Hsp90 responding to client interaction. Nature Communications. 9: 1472. PMID 29662162 DOI: 10.1038/S41467-018-03946-X |
0.482 |
|
| 2018 |
Rosam M, Krader D, Nickels C, Hochmair J, Back KC, Agam G, Barth A, Zeymer C, Hendrix J, Schneider M, Antes I, Reinstein J, Lamb DC, Buchner J. Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate. Nature Structural & Molecular Biology. 25: 90-100. PMID 29323281 DOI: 10.1038/S41594-017-0012-6 |
0.443 |
|
| 2018 |
Jahn M, Tych K, Girstmair H, Steinmaßl M, Hugel T, Buchner J, Rief M. Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. Structure (London, England : 1993). 26: 96-105.e4. PMID 29276035 DOI: 10.1016/J.Str.2017.11.023 |
0.489 |
|
| 2018 |
Weber B, Berner C, Feind G, Buchner J, Brandl M, Pradhan T, Reif B, Cendales MDP, Zacharias M. Backbone 1H, 15N, 13C chemical shift assignments for MAK33 EV-CH2-SK antibody domain extended variant Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27585 |
0.32 |
|
| 2018 |
Weber B, Berner C, Feind G, Buchner J, Brandl M, Pradhan T, Reif B, Cendales MDP, Zacharias M. Backbone 1H, 15N, 13C chemical shift assignments for the MAK33 CH2 antibody domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27584 |
0.316 |
|
| 2017 |
Pasalic D, Weber B, Giannone C, Anelli T, Müller R, Fagioli C, Felkl M, John C, Mossuto MF, Becker CFW, Sitia R, Buchner J. A peptide extension dictates IgM assembly. Proceedings of the National Academy of Sciences of the United States of America. PMID 28973899 DOI: 10.1073/Pnas.1701797114 |
0.37 |
|
| 2017 |
Herold EM, John C, Weber B, Kremser S, Eras J, Berner C, Deubler S, Zacharias M, Buchner J. Determinants of the assembly and function of antibody variable domains. Scientific Reports. 7: 12276. PMID 28947772 DOI: 10.1038/S41598-017-12519-9 |
0.401 |
|
| 2017 |
Sahasrabudhe P, Rohrberg J, Biebl MM, Rutz DA, Buchner J. The Plasticity of the Hsp90 Co-chaperone System. Molecular Cell. PMID 28890336 DOI: 10.1016/J.Molcel.2017.08.004 |
0.459 |
|
| 2017 |
Stiegler SC, Rübbelke M, Korotkov VS, Weiwad M, John C, Fischer G, Sieber SA, Sattler M, Buchner J. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex. The Journal of Biological Chemistry. PMID 28851842 DOI: 10.1074/Jbc.M117.797829 |
0.442 |
|
| 2017 |
Hora M, Sarkar R, Morris V, Xue K, Prade E, Harding E, Buchner J, Reif B. MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors. Plos One. 12: e0181799. PMID 28746363 DOI: 10.1371/Journal.Pone.0181799 |
0.382 |
|
| 2017 |
Schopf FH, Biebl MM, Buchner J. The HSP90 chaperone machinery. Nature Reviews. Molecular Cell Biology. PMID 28429788 DOI: 10.1038/Nrm.2017.20 |
0.459 |
|
| 2017 |
Gade Malmos K, Blancas-Mejia LM, Weber B, Buchner J, Ramirez-Alvarado M, Naiki H, Otzen D. ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-16. PMID 28393556 DOI: 10.1080/13506129.2017.1304905 |
0.331 |
|
| 2017 |
Schuster M, Schnell L, Feigl P, Birkhofer C, Mohr K, Roeder M, Carle S, Langer S, Tippel F, Buchner J, Fischer G, Hausch F, Frick M, Schwan C, Aktories K, et al. The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells. Scientific Reports. 7: 613. PMID 28377614 DOI: 10.1038/S41598-017-00780-X |
0.4 |
|
| 2017 |
Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W, Bartelt-Kirbach B, Brundel BJ, Buchner J, Bukau B, Carver JA, Ecroyd H, Emanuelsson C, Finet S, Golenhofen N, et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress & Chaperones. PMID 28364346 DOI: 10.1007/S12192-017-0787-8 |
0.439 |
|
| 2017 |
Luo Q, Boczek EE, Wang Q, Buchner J, Kaila VR. Hsp90 dependence of a kinase is determined by its conformational landscape. Scientific Reports. 7: 43996. PMID 28290541 DOI: 10.1038/Srep43996 |
0.41 |
|
| 2017 |
Preis W, Bestehorn A, Buchner J, Haslbeck M. An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins. Cell Stress & Chaperones. PMID 28214988 DOI: 10.1007/S12192-017-0772-2 |
0.418 |
|
| 2017 |
Hora M, Carballo-Pacheco M, Weber B, Morris VK, Wittkopf A, Buchner J, Strodel B, Reif B. Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains. Scientific Reports. 7: 41515. PMID 28128355 DOI: 10.1038/Srep41515 |
0.381 |
|
| 2017 |
Ambrosius D, Buchner J, Feige MJ. Wir brauchen eine next generation protein science in Deutschland Biospektrum. 23: 793-793. DOI: 10.1007/S12268-017-0863-8 |
0.342 |
|
| 2016 |
Buchner J, Eisenberg D, Schmid F. In memoriam - Rainer Jaenicke. Protein Science : a Publication of the Protein Society. PMID 27977893 DOI: 10.1002/Pro.3098 |
0.502 |
|
| 2016 |
Mymrikov EV, Daake M, Richter B, Haslbeck M, Buchner J. The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins. The Journal of Biological Chemistry. PMID 27909051 DOI: 10.1074/Jbc.M116.760413 |
0.47 |
|
| 2016 |
Zierer BK, Rübbelke M, Tippel F, Madl T, Schopf FH, Rutz DA, Richter K, Sattler M, Buchner J. Importance of cycle timing for the function of the molecular chaperone Hsp90. Nature Structural & Molecular Biology. PMID 27723736 DOI: 10.1038/Nsmb.3305 |
0.465 |
|
| 2016 |
Rehn A, Moroni E, Zierer BK, Tippel F, Morra G, John C, Richter K, Colombo G, Buchner J. Allosteric regulation points control the conformational dynamics of the molecular chaperone Hsp90. Journal of Molecular Biology. PMID 27663270 DOI: 10.1016/J.Jmb.2016.09.014 |
0.42 |
|
| 2016 |
Dashivets T, Stracke J, Dengl S, Knaupp A, Pollmann J, Buchner J, Schlothauer T. Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies. Mabs. 0. PMID 27612038 DOI: 10.1080/19420862.2016.1231277 |
0.326 |
|
| 2016 |
Hoseini H, Pandey S, Jores T, Schmitt A, Franz-Wachtel M, Macek B, Buchner J, Dimmer KS, Rapaport D. The cytosolic co-chaperone Sti1 is relevant for mitochondrial biogenesis and morphology. The Febs Journal. PMID 27412066 DOI: 10.1111/Febs.13813 |
0.373 |
|
| 2016 |
Schneider M, Rosam M, Glaser M, Patronov A, Shah H, Back KC, Daake MA, Buchner J, Antes I. BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP. Proteins. PMID 27287023 DOI: 10.1002/Prot.25084 |
0.32 |
|
| 2016 |
Nokwe CN, Hora M, Zacharias M, Yagi H, Peschek J, Reif B, Goto Y, Buchner J. Specific non-native interactions. Journal of Molecular Biology. PMID 26827727 DOI: 10.1016/J.Jmb.2016.01.015 |
0.414 |
|
| 2016 |
Jahn M, Buchner J, Hugel T, Rief M. Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments. Proceedings of the National Academy of Sciences of the United States of America. PMID 26787848 DOI: 10.1073/Pnas.1518827113 |
0.491 |
|
| 2016 |
Wengler D, Rosam M, Hendrix J, Buchner J, Lamb DC. Studying the Function of BAP in the Nucleotide Cycle of BIP by spFRET using MFD-PIE Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.1007 |
0.504 |
|
| 2015 |
Dashivets T, Thomann M, Rueger P, Knaupp A, Buchner J, Schlothauer T. Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants. Plos One. 10: e0143520. PMID 26657484 DOI: 10.1371/Journal.Pone.0143520 |
0.326 |
|
| 2015 |
Mainz A, Peschek J, Stavropoulou M, Back KC, Bardiaux B, Asami S, Prade E, Peters C, Weinkauf S, Buchner J, Reif B. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client. Nature Structural & Molecular Biology. PMID 26458046 DOI: 10.1038/Nsmb.3108 |
0.487 |
|
| 2015 |
Nokwe CN, Hora M, Zacharias M, Yagi H, John C, Reif B, Goto Y, Buchner J. The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation. Journal of Molecular Biology. 427: 3572-86. PMID 26408269 DOI: 10.1016/J.Jmb.2015.09.012 |
0.432 |
|
| 2015 |
Haslbeck M, Peschek J, Buchner J, Weinkauf S. Structure and function of α-crystallins: Traversing from in vitro to in vivo. Biochimica Et Biophysica Acta. PMID 26116912 DOI: 10.1016/J.Bbagen.2015.06.008 |
0.347 |
|
| 2015 |
Boczek EE, Reefschläger LG, Dehling M, Struller TJ, Häusler E, Seidl A, Kaila VR, Buchner J. Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90. Proceedings of the National Academy of Sciences of the United States of America. 112: E3189-98. PMID 26056257 DOI: 10.1073/Pnas.1424342112 |
0.341 |
|
| 2015 |
Fleckenstein T, Kastenmüller A, Stein ML, Peters C, Daake M, Krause M, Weinfurtner D, Haslbeck M, Weinkauf S, Groll M, Buchner J. The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes. Molecular Cell. 58: 1067-78. PMID 26009280 DOI: 10.1016/J.Molcel.2015.04.019 |
0.417 |
|
| 2015 |
Röhl A, Wengler D, Madl T, Lagleder S, Tippel F, Herrmann M, Hendrix J, Richter K, Hack G, Schmid AB, Kessler H, Lamb DC, Buchner J. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. Nature Communications. 6: 6655. PMID 25851214 DOI: 10.1038/Ncomms7655 |
0.414 |
|
| 2015 |
Haslbeck M, Buchner J. Assays to characterize molecular chaperone function in vitro. Methods in Molecular Biology (Clifton, N.J.). 1292: 39-51. PMID 25804746 DOI: 10.1007/978-1-4939-2522-3_3 |
0.393 |
|
| 2015 |
Huang B, Lucas T, Kueppers C, Dong X, Krause M, Bepperling A, Buchner J, Voshol H, Weiss A, Gerrits B, Kochanek S. Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin. Plos One. 10: e0121055. PMID 25799558 DOI: 10.1371/Journal.Pone.0121055 |
0.381 |
|
| 2015 |
Röhl A, Tippel F, Bender E, Schmid AB, Richter K, Madl T, Buchner J. Hop/Sti1 phosphorylation inhibits its co-chaperone function. Embo Reports. 16: 240-9. PMID 25504578 DOI: 10.15252/Embr.201439198 |
0.431 |
|
| 2015 |
Rehn AB, Buchner J. p23 and Aha1. Sub-Cellular Biochemistry. 78: 113-31. PMID 25487019 DOI: 10.1007/978-3-319-11731-7_6 |
0.447 |
|
| 2014 |
Jahn M, Rehn A, Pelz B, Hellenkamp B, Richter K, Rief M, Buchner J, Hugel T. The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. Proceedings of the National Academy of Sciences of the United States of America. 111: 17881-6. PMID 25468961 DOI: 10.1073/Pnas.1414073111 |
0.453 |
|
| 2014 |
Alvira S, Cuéllar J, Röhl A, Yamamoto S, Itoh H, Alfonso C, Rivas G, Buchner J, Valpuesta JM. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. Nature Communications. 5: 5484. PMID 25407331 DOI: 10.1038/Ncomms6484 |
0.473 |
|
| 2014 |
Girstmair H, Buchner J. GET two for one. Molecular Cell. 56: 1-2. PMID 25280098 DOI: 10.1016/J.Molcel.2014.09.015 |
0.325 |
|
| 2014 |
Zierer BK, Weiwad M, Rübbelke M, Freiburger L, Fischer G, Lorenz OR, Sattler M, Richter K, Buchner J. Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions. Angewandte Chemie (International Ed. in English). 53: 12257-62. PMID 25244159 DOI: 10.1002/Anie.201406578 |
0.417 |
|
| 2014 |
Nokwe CN, Zacharias M, Yagi H, Hora M, Reif B, Goto Y, Buchner J. A residue-specific shift in stability and amyloidogenicity of antibody variable domains. The Journal of Biological Chemistry. 289: 26829-46. PMID 25096580 DOI: 10.1074/Jbc.M114.582247 |
0.404 |
|
| 2014 |
Buchner J, Kessler H. Protein folding by interaction. Structure (London, England : 1993). 22: 936-7. PMID 25007223 DOI: 10.1016/J.Str.2014.06.006 |
0.441 |
|
| 2014 |
Feige MJ, Buchner J. Principles and engineering of antibody folding and assembly. Biochimica Et Biophysica Acta. 1844: 2024-2031. PMID 24931831 DOI: 10.1016/J.Bbapap.2014.06.004 |
0.394 |
|
| 2014 |
Feige MJ, Gräwert MA, Marcinowski M, Hennig J, Behnke J, Ausländer D, Herold EM, Peschek J, Castro CD, Flajnik M, Hendershot LM, Sattler M, Groll M, Buchner J. The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins. Proceedings of the National Academy of Sciences of the United States of America. 111: 8155-60. PMID 24830426 DOI: 10.1073/Pnas.1321502111 |
0.403 |
|
| 2014 |
Paul A, Garcia YA, Zierer B, Patwardhan C, Gutierrez O, Hildenbrand Z, Harris DC, Balsiger HA, Sivils JC, Johnson JL, Buchner J, Chadli A, Cox MB. The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors. The Journal of Biological Chemistry. 289: 15297-308. PMID 24753260 DOI: 10.1074/Jbc.M113.535229 |
0.369 |
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| 2014 |
Lorenz OR, Freiburger L, Rutz DA, Krause M, Zierer BK, Alvira S, Cuéllar J, Valpuesta JM, Madl T, Sattler M, Buchner J. Modulation of the Hsp90 chaperone cycle by a stringent client protein. Molecular Cell. 53: 941-53. PMID 24613341 DOI: 10.1016/J.Molcel.2014.02.003 |
0.445 |
|
| 2014 |
Zierer BK, Weiwad M, Rübbelke M, Freiburger L, Fischer G, Lorenz OR, Sattler M, Richter K, Buchner J. Aktivatoren des molekularen Chaperons Hsp90 erleichtern geschwindigkeitsbestimmende Konformationsänderungen Angewandte Chemie. 126: 12454-12459. DOI: 10.1002/Ange.201406578 |
0.377 |
|
| 2013 |
Kayser J, Haslbeck M, Dempfle L, Krause M, Grashoff C, Buchner J, Herrmann H, Bausch AR. The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biophysical Journal. 105: 1778-85. PMID 24138853 DOI: 10.1016/J.Bpj.2013.09.007 |
0.38 |
|
| 2013 |
Peschek J, Braun N, Rohrberg J, Back KC, Kriehuber T, Kastenmüller A, Weinkauf S, Buchner J. Regulated structural transitions unleash the chaperone activity of αB-crystallin. Proceedings of the National Academy of Sciences of the United States of America. 110: E3780-9. PMID 24043785 DOI: 10.1073/Pnas.1308898110 |
0.496 |
|
| 2013 |
Bertz M, Buchner J, Rief M. Mechanical stability of the antibody domain CH3 homodimer in different oxidation states. Journal of the American Chemical Society. 135: 15085-91. PMID 24015948 DOI: 10.1021/Ja405076J |
0.348 |
|
| 2013 |
Beebe K, Mollapour M, Scroggins B, Prodromou C, Xu W, Tokita M, Taldone T, Pullen L, Zierer BK, Lee MJ, Trepel J, Buchner J, Bolon D, Chiosis G, Neckers L. Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors. Oncotarget. 4: 1065-74. PMID 23867252 DOI: 10.18632/Oncotarget.1099 |
0.479 |
|
| 2013 |
Li J, Buchner J. Structure, function and regulation of the hsp90 machinery. Biomedical Journal. 36: 106-17. PMID 23806880 DOI: 10.4103/2319-4170.113230 |
0.525 |
|
| 2013 |
Hendershot LM, Feige MJ, Buchner J. Acidification activates ERp44--a molecular litmus test for protein assembly. Molecular Cell. 50: 779-81. PMID 23806332 DOI: 10.1016/J.Molcel.2013.06.008 |
0.378 |
|
| 2013 |
Müller R, Gräwert MA, Kern T, Madl T, Peschek J, Sattler M, Groll M, Buchner J. High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation. Proceedings of the National Academy of Sciences of the United States of America. 110: 10183-8. PMID 23733956 DOI: 10.1073/Pnas.1300547110 |
0.325 |
|
| 2013 |
Röhl A, Rohrberg J, Buchner J. The chaperone Hsp90: changing partners for demanding clients. Trends in Biochemical Sciences. 38: 253-62. PMID 23507089 DOI: 10.1016/J.Tibs.2013.02.003 |
0.481 |
|
| 2013 |
Li J, Zoldak G, Kriehuber T, Soroka J, Schmid FX, Richter K, Buchner J. Unique proline-rich domain regulates the chaperone function of AIPL1. Biochemistry. 52: 2089-96. PMID 23418749 DOI: 10.1021/Bi301648Q |
0.657 |
|
| 2013 |
Li J, Richter K, Reinstein J, Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nature Structural & Molecular Biology. 20: 326-31. PMID 23396352 DOI: 10.1038/Nsmb.2502 |
0.439 |
|
| 2013 |
Kateb F, Perrin H, Tripsianes K, Zou P, Spadaccini R, Bottomley M, Franzmann TM, Buchner J, Ansieau S, Sattler M. Structural and functional analysis of the DEAF-1 and BS69 MYND domains. Plos One. 8: e54715. PMID 23372760 DOI: 10.1371/Journal.Pone.0054715 |
0.437 |
|
| 2013 |
Marcinowski M, Rosam M, Seitz C, Elferich J, Behnke J, Bello C, Feige MJ, Becker CF, Antes I, Buchner J. Conformational selection in substrate recognition by Hsp70 chaperones. Journal of Molecular Biology. 425: 466-74. PMID 23207294 DOI: 10.1016/J.Jmb.2012.11.030 |
0.443 |
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| 2013 |
Retzlaff M, Rohrberg J, Küpper NJ, Lagleder S, Bepperling A, Manzenrieder F, Peschek J, Kessler H, Buchner J. The regulatory domain stabilizes the p53 tetramer by intersubunit contacts with the DNA binding domain. Journal of Molecular Biology. 425: 144-55. PMID 23103206 DOI: 10.1016/J.Jmb.2012.10.015 |
0.369 |
|
| 2012 |
Bepperling A, Alte F, Kriehuber T, Braun N, Weinkauf S, Groll M, Haslbeck M, Buchner J. Alternative bacterial two-component small heat shock protein systems. Proceedings of the National Academy of Sciences of the United States of America. 109: 20407-12. PMID 23184973 DOI: 10.1073/Pnas.1209565109 |
0.484 |
|
| 2012 |
Soroka J, Buchner J. Mechanistic aspects of the Hsp90 phosphoregulation. Cell Cycle (Georgetown, Tex.). 11: 1870-1. PMID 22544316 DOI: 10.4161/Cc.20418 |
0.359 |
|
| 2012 |
Schreiber TB, Mäusbacher N, Soroka J, Wandinger SK, Buchner J, Daub H. Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae. Journal of Proteome Research. 11: 2397-408. PMID 22369663 DOI: 10.1021/Pr201134P |
0.373 |
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| 2012 |
Soroka J, Wandinger SK, Mäusbacher N, Schreiber T, Richter K, Daub H, Buchner J. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Molecular Cell. 45: 517-28. PMID 22365831 DOI: 10.1016/J.Molcel.2011.12.031 |
0.429 |
|
| 2012 |
Schmid AB, Lagleder S, Gräwert MA, Röhl A, Hagn F, Wandinger SK, Cox MB, Demmer O, Richter K, Groll M, Kessler H, Buchner J. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. The Embo Journal. 31: 1506-17. PMID 22227520 DOI: 10.1038/Emboj.2011.472 |
0.478 |
|
| 2012 |
Li J, Soroka J, Buchner J. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochimica Et Biophysica Acta. 1823: 624-35. PMID 21951723 DOI: 10.1016/J.Bbamcr.2011.09.003 |
0.467 |
|
| 2012 |
Schmid A, Lagleder S, Graewert M, Roehl A, Hagn F, Wandinger S, Cox M, Demmer O, Richter K, Groll M, Kessler H, Buchner J. Solution structure of the yeast Sti1 DP1 domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Llv/Pdb |
0.322 |
|
| 2012 |
Kayser J, Haslbeck M, Herrmann H, Buchner J, Bausch AR. Heat Shock Proteins Regulate Structure of Intermediate Filament Networks Biophysical Journal. 102: 6-6. DOI: 10.1016/J.Bpj.2011.11.3775 |
0.35 |
|
| 2012 |
Horwich AL, Buchner J, Smock RG, Gierasch LM, Saibil HR. Chaperones and protein folding Comprehensive Biophysics. 3: 212-237. DOI: 10.1016/B978-0-12-374920-8.00313-1 |
0.353 |
|
| 2011 |
Braun N, Zacharias M, Peschek J, Kastenmüller A, Zou J, Hanzlik M, Haslbeck M, Rappsilber J, Buchner J, Weinkauf S. Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proceedings of the National Academy of Sciences of the United States of America. 108: 20491-6. PMID 22143763 DOI: 10.1073/Pnas.1111014108 |
0.347 |
|
| 2011 |
Hagn F, Lagleder S, Retzlaff M, Rohrberg J, Demmer O, Richter K, Buchner J, Kessler H. Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nature Structural & Molecular Biology. 18: 1086-93. PMID 21892170 DOI: 10.1038/Nsmb.2114 |
0.464 |
|
| 2011 |
Kaiser E, Kroll C, Ernst K, Schwan C, Popoff M, Fischer G, Buchner J, Aktories K, Barth H. Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infection and Immunity. 79: 3913-21. PMID 21768281 DOI: 10.1128/Iai.05372-11 |
0.384 |
|
| 2011 |
Richter K, Buchner J. Closing in on the Hsp90 chaperone-client relationship. Structure (London, England : 1993). 19: 445-6. PMID 21481768 DOI: 10.1016/J.Str.2011.03.007 |
0.424 |
|
| 2011 |
Marcinowski M, Höller M, Feige MJ, Baerend D, Lamb DC, Buchner J. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature Structural & Molecular Biology. 18: 150-8. PMID 21217698 DOI: 10.1038/Nsmb.1970 |
0.497 |
|
| 2011 |
Li J, Richter K, Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nature Structural & Molecular Biology. 18: 61-6. PMID 21170051 DOI: 10.1038/Nsmb.1965 |
0.418 |
|
| 2011 |
Dmochewitz L, Lillich M, Kaiser E, Jennings LD, Lang AE, Buchner J, Fischer G, Aktories K, Collier RJ, Barth H. Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen. Cellular Microbiology. 13: 359-73. PMID 20946244 DOI: 10.1111/J.1462-5822.2010.01539.X |
0.37 |
|
| 2011 |
Hagn F, Retzlaff M, Rohrberg J, Buchner J, Kessler H. Backbone 1H, 13C, and 15N Chemical Shift Assignments for the yeast Hsp90 Middle Domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16279 |
0.384 |
|
| 2010 |
Richter K, Haslbeck M, Buchner J. The heat shock response: life on the verge of death. Molecular Cell. 40: 253-66. PMID 20965420 DOI: 10.1016/J.Molcel.2010.10.006 |
0.407 |
|
| 2010 |
Anselment B, Baerend D, Mey E, Buchner J, Weuster-Botz D, Haslbeck M. Experimental optimization of protein refolding with a genetic algorithm. Protein Science : a Publication of the Protein Society. 19: 2085-95. PMID 20799347 DOI: 10.1002/Pro.488 |
0.326 |
|
| 2010 |
Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Molecular Cell. 39: 507-20. PMID 20797624 DOI: 10.1016/J.Molcel.2010.08.001 |
0.366 |
|
| 2010 |
Ratzke C, Mickler M, Hellenkamp B, Buchner J, Hugel T. Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proceedings of the National Academy of Sciences of the United States of America. 107: 16101-6. PMID 20736353 DOI: 10.1073/Pnas.1000916107 |
0.497 |
|
| 2010 |
Bertz M, Chen J, Feige MJ, Franzmann TM, Buchner J, Rief M. Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5. Journal of Molecular Biology. 400: 1046-56. PMID 20595041 DOI: 10.1016/J.Jmb.2010.05.065 |
0.464 |
|
| 2010 |
Kriehuber T, Rattei T, Weinmaier T, Bepperling A, Haslbeck M, Buchner J. Independent evolution of the core domain and its flanking sequences in small heat shock proteins. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 24: 3633-42. PMID 20501794 DOI: 10.1096/Fj.10-156992 |
0.458 |
|
| 2010 |
Feige MJ, Simpson ER, Herold EM, Bepperling A, Heger K, Buchner J. Dissecting the alternatively folded state of the antibody Fab fragment. Journal of Molecular Biology. 399: 719-30. PMID 20434459 DOI: 10.1016/J.Jmb.2010.04.032 |
0.413 |
|
| 2010 |
Rudolph B, Gebendorfer KM, Buchner J, Winter J. Evolution of Escherichia coli for growth at high temperatures. The Journal of Biological Chemistry. 285: 19029-34. PMID 20406805 DOI: 10.1074/Jbc.M110.103374 |
0.312 |
|
| 2010 |
Echeverria PC, Figueras MJ, Vogler M, Kriehuber T, de Miguel N, Deng B, Dalmasso MC, Matthews DE, Matrajt M, Haslbeck M, Buchner J, Angel SO. The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination. Molecular and Biochemical Parasitology. 172: 129-40. PMID 20403389 DOI: 10.1016/J.Molbiopara.2010.04.004 |
0.398 |
|
| 2010 |
Buchner J. Bacterial Hsp90--desperately seeking clients. Molecular Microbiology. 76: 540-4. PMID 20345652 DOI: 10.1111/J.1365-2958.2010.07140.X |
0.321 |
|
| 2010 |
Chen J, Feige MJ, Franzmann TM, Bepperling A, Buchner J. Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization. Journal of Molecular Biology. 398: 122-31. PMID 20171228 DOI: 10.1016/J.Jmb.2010.02.022 |
0.436 |
|
| 2010 |
Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J. Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Molecular Cell. 37: 344-54. PMID 20159554 DOI: 10.1016/J.Molcel.2010.01.006 |
0.495 |
|
| 2010 |
Jinwal UK, Koren J, Borysov SI, Schmid AB, Abisambra JF, Blair LJ, Johnson AG, Jones JR, Shults CL, O'Leary JC, Jin Y, Buchner J, Cox MB, Dickey CA. The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 30: 591-9. PMID 20071522 DOI: 10.1523/Jneurosci.4815-09.2010 |
0.427 |
|
| 2010 |
Feige MJ, Hendershot LM, Buchner J. How antibodies fold. Trends in Biochemical Sciences. 35: 189-98. PMID 20022755 DOI: 10.1016/J.Tibs.2009.11.005 |
0.437 |
|
| 2010 |
Feige MJ, Hendershot LM, Buchner J. Response to Corcos: exceptions to the rules Trends in Biochemical Sciences. 35: 594. DOI: 10.1016/J.Tibs.2010.07.011 |
0.365 |
|
| 2010 |
Hugel T, Ratzke C, Mickler M, Hessling M, Buchner J. Coordination between N- and C-terminal Kinetics of Hsp90 Investigated by SmFRET Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.3451 |
0.421 |
|
| 2009 |
Tsutsumi S, Mollapour M, Graf C, Lee CT, Scroggins BT, Xu W, Haslerova L, Hessling M, Konstantinova AA, Trepel JB, Panaretou B, Buchner J, Mayer MP, Prodromou C, Neckers L. Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nature Structural & Molecular Biology. 16: 1141-7. PMID 19838189 DOI: 10.1038/Nsmb.1682 |
0.415 |
|
| 2009 |
Müller M, Richter K, Heuck A, Kremmer E, Buchner J, Jansen RP, Niessing D. Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization. Rna (New York, N.Y.). 15: 2002-12. PMID 19710186 DOI: 10.1261/Rna.1753309 |
0.336 |
|
| 2009 |
de Miguel N, Braun N, Bepperling A, Kriehuber T, Kastenmüller A, Buchner J, Angel SO, Haslbeck M. Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii. Biochimica Et Biophysica Acta. 1793: 1738-48. PMID 19699241 DOI: 10.1016/J.Bbamcr.2009.08.005 |
0.44 |
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| 2009 |
Retzlaff M, Stahl M, Eberl HC, Lagleder S, Beck J, Kessler H, Buchner J. Hsp90 is regulated by a switch point in the C-terminal domain. Embo Reports. 10: 1147-53. PMID 19696785 DOI: 10.1038/Embor.2009.153 |
0.49 |
|
| 2009 |
Peschek J, Braun N, Franzmann TM, Georgalis Y, Haslbeck M, Weinkauf S, Buchner J. The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proceedings of the National Academy of Sciences of the United States of America. 106: 13272-7. PMID 19651604 DOI: 10.1073/Pnas.0902651106 |
0.335 |
|
| 2009 |
Simpson ER, Herold EM, Buchner J. The folding pathway of the antibody V(L) domain. Journal of Molecular Biology. 392: 1326-38. PMID 19647749 DOI: 10.1016/J.Jmb.2009.07.075 |
0.443 |
|
| 2009 |
Feige MJ, Nath S, Catharino SR, Weinfurtner D, Steinbacher S, Buchner J. Structure of the murine unglycosylated IgG1 Fc fragment. Journal of Molecular Biology. 391: 599-608. PMID 19559712 DOI: 10.1016/J.Jmb.2009.06.048 |
0.765 |
|
| 2009 |
Hainzl O, Lapina MC, Buchner J, Richter K. The charged linker region is an important regulator of Hsp90 function. The Journal of Biological Chemistry. 284: 22559-67. PMID 19553666 DOI: 10.1074/Jbc.M109.031658 |
0.477 |
|
| 2009 |
Feige MJ, Groscurth S, Marcinowski M, Shimizu Y, Kessler H, Hendershot LM, Buchner J. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Molecular Cell. 34: 569-79. PMID 19524537 DOI: 10.1016/J.Molcel.2009.04.028 |
0.432 |
|
| 2009 |
Dashivets T, Wood N, Hergersberg C, Buchner J, Haslbeck M. Rapid matrix-assisted refolding of histidine-tagged proteins. Chembiochem : a European Journal of Chemical Biology. 10: 869-76. PMID 19235820 DOI: 10.1002/Cbic.200800697 |
0.405 |
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| 2009 |
Mickler M, Hessling M, Ratzke C, Buchner J, Hugel T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nature Structural & Molecular Biology. 16: 281-6. PMID 19234469 DOI: 10.1038/Nsmb.1557 |
0.432 |
|
| 2009 |
Hessling M, Richter K, Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nature Structural & Molecular Biology. 16: 287-93. PMID 19234467 DOI: 10.1038/Nsmb.1565 |
0.415 |
|
| 2009 |
Pandya MJ, Bendz H, Manzenrieder F, Noessner E, Kessler H, Buchner J, Issels RD. Interaction of human heat shock protein 70 with tumor-associated peptides. Biological Chemistry. 390: 305-12. PMID 19199830 DOI: 10.1515/Bc.2009.038 |
0.345 |
|
| 2009 |
Hagn F, Retzlaff M, Mitschke L, Hessling M, Gugel F, Richter K, Buchner J, Kessler H. NMR Assignment of the C-terminal Domain of yeast Aha-1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16588 |
0.362 |
|
| 2008 |
Feige MJ, Groscurth S, Marcinowski M, Yew ZT, Truffault V, Paci E, Kessler H, Buchner J. The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity. Proceedings of the National Academy of Sciences of the United States of America. 105: 13373-8. PMID 18768806 DOI: 10.1073/Pnas.0802809105 |
0.444 |
|
| 2008 |
Schmid K, Haslbeck M, Buchner J, Somoza V. Induction of heat shock proteins and the proteasome system by casein-N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)lysine in Caco-2 cells. Annals of the New York Academy of Sciences. 1126: 257-61. PMID 18448826 DOI: 10.1196/Annals.1433.062 |
0.432 |
|
| 2008 |
Wandinger SK, Richter K, Buchner J. The Hsp90 chaperone machinery. The Journal of Biological Chemistry. 283: 18473-7. PMID 18442971 DOI: 10.1074/Jbc.R800007200 |
0.382 |
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| 2008 |
Richter K, Soroka J, Skalniak L, Leskovar A, Hessling M, Reinstein J, Buchner J. Conserved conformational changes in the ATPase cycle of human Hsp90. The Journal of Biological Chemistry. 283: 17757-65. PMID 18400751 DOI: 10.1074/Jbc.M800540200 |
0.485 |
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| 2008 |
Haslbeck M, Kastenmüller A, Buchner J, Weinkauf S, Braun N. Structural dynamics of archaeal small heat shock proteins. Journal of Molecular Biology. 378: 362-74. PMID 18353362 DOI: 10.1016/J.Jmb.2008.01.095 |
0.443 |
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| 2008 |
Leskovar A, Wegele H, Werbeck ND, Buchner J, Reinstein J. The ATPase cycle of the mitochondrial Hsp90 analog Trap1. The Journal of Biological Chemistry. 283: 11677-88. PMID 18287101 DOI: 10.1074/Jbc.M709516200 |
0.384 |
|
| 2008 |
Franzmann TM, Menhorn P, Walter S, Buchner J. Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. Molecular Cell. 29: 207-16. PMID 18243115 DOI: 10.1016/J.Molcel.2007.11.025 |
0.408 |
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| 2008 |
Frey S, Haslbeck M, Hainzl O, Buchner J. Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system. Biological Chemistry. 389: 37-45. PMID 18095868 DOI: 10.1515/Bc.2008.007 |
0.351 |
|
| 2008 |
Buchner J, Kiefhaber T. Protein Folding Handbook Protein Folding Handbook. 1: 1-1333. DOI: 10.1002/9783527619498 |
0.637 |
|
| 2007 |
Heuck A, Du TG, Jellbauer S, Richter K, Kruse C, Jaklin S, Müller M, Buchner J, Jansen RP, Niessing D. Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes. Proceedings of the National Academy of Sciences of the United States of America. 104: 19778-83. PMID 18056806 DOI: 10.1073/Pnas.0706780104 |
0.368 |
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| 2007 |
Richter K, Reinstein J, Buchner J. A Grp on the Hsp90 mechanism. Molecular Cell. 28: 177-9. PMID 17964255 DOI: 10.1016/J.Molcel.2007.10.007 |
0.338 |
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| 2007 |
Riggs DL, Cox MB, Tardif HL, Hessling M, Buchner J, Smith DF. Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling. Molecular and Cellular Biology. 27: 8658-69. PMID 17938211 DOI: 10.1128/Mcb.00985-07 |
0.349 |
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| 2007 |
Frey S, Leskovar A, Reinstein J, Buchner J. The ATPase cycle of the endoplasmic chaperone Grp94. The Journal of Biological Chemistry. 282: 35612-20. PMID 17925398 DOI: 10.1074/Jbc.M704647200 |
0.434 |
|
| 2007 |
Janig E, Haslbeck M, Aigelsreiter A, Braun N, Unterthor D, Wolf P, Khaskhely NM, Buchner J, Denk H, Zatloukal K. Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from ultraviolet-induced aggregation in vitro. The American Journal of Pathology. 171: 1474-82. PMID 17872975 DOI: 10.2353/Ajpath.2007.061064 |
0.346 |
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| 2007 |
Cox MB, Riggs DL, Hessling M, Schumacher F, Buchner J, Smith DF. FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity. Molecular Endocrinology (Baltimore, Md.). 21: 2956-67. PMID 17717070 DOI: 10.1210/Me.2006-0547 |
0.413 |
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| 2007 |
Bendz H, Ruhland SC, Pandya MJ, Hainzl O, Riegelsberger S, Braüchle C, Mayer MP, Buchner J, Issels RD, Noessner E. Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. The Journal of Biological Chemistry. 282: 31688-702. PMID 17684010 DOI: 10.1074/Jbc.M704129200 |
0.369 |
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| 2007 |
Feige MJ, Hagn F, Esser J, Kessler H, Buchner J. Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. Journal of Molecular Biology. 365: 1232-44. PMID 17112539 DOI: 10.1016/J.Jmb.2006.10.049 |
0.485 |
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| 2006 |
Richter K, Buchner J. hsp90: twist and fold. Cell. 127: 251-3. PMID 17055424 DOI: 10.1016/J.Cell.2006.10.004 |
0.37 |
|
| 2006 |
White HE, Orlova EV, Chen S, Wang L, Ignatiou A, Gowen B, Stromer T, Franzmann TM, Haslbeck M, Buchner J, Saibil HR. Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure (London, England : 1993). 14: 1197-204. PMID 16843901 DOI: 10.1016/J.Str.2006.05.021 |
0.495 |
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| 2006 |
Scheibel T, Buchner J. Protein aggregation as a cause for disease. Handbook of Experimental Pharmacology. 199-219. PMID 16610361 DOI: 10.1007/3-540-29717-0_9 |
0.595 |
|
| 2006 |
Richter K, Moser S, Hagn F, Friedrich R, Hainzl O, Heller M, Schlee S, Kessler H, Reinstein J, Buchner J. Intrinsic inhibition of the Hsp90 ATPase activity. The Journal of Biological Chemistry. 281: 11301-11. PMID 16461354 DOI: 10.1074/Jbc.M510142200 |
0.501 |
|
| 2006 |
Wandinger SK, Suhre MH, Wegele H, Buchner J. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. The Embo Journal. 25: 367-76. PMID 16407978 DOI: 10.1038/Sj.Emboj.7600930 |
0.496 |
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| 2006 |
Wegele H, Wandinger SK, Schmid AB, Reinstein J, Buchner J. Substrate transfer from the chaperone Hsp70 to Hsp90. Journal of Molecular Biology. 356: 802-11. PMID 16403523 DOI: 10.1016/J.Jmb.2005.12.008 |
0.485 |
|
| 2005 |
Shaner L, Wegele H, Buchner J, Morano KA. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. The Journal of Biological Chemistry. 280: 41262-9. PMID 16221677 DOI: 10.1074/Jbc.M503614200 |
0.456 |
|
| 2005 |
Catharino S, Buchner J, Walter S. Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p. Biological Chemistry. 386: 633-41. PMID 16207084 DOI: 10.1515/Bc.2005.074 |
0.775 |
|
| 2005 |
Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. Some like it hot: the structure and function of small heat-shock proteins. Nature Structural & Molecular Biology. 12: 842-6. PMID 16205709 DOI: 10.1038/Nsmb993 |
0.484 |
|
| 2005 |
Dehner A, Klein C, Hansen S, Müller L, Buchner J, Schwaiger M, Kessler H. Cooperative binding of p53 to DNA: regulation by protein-protein interactions through a double salt bridge. Angewandte Chemie (International Ed. in English). 44: 5247-51. PMID 16035029 DOI: 10.1002/Anie.200501887 |
0.377 |
|
| 2005 |
Franzmann TM, Wühr M, Richter K, Walter S, Buchner J. The activation mechanism of Hsp26 does not require dissociation of the oligomer. Journal of Molecular Biology. 350: 1083-93. PMID 15967461 DOI: 10.1016/J.Jmb.2005.05.034 |
0.538 |
|
| 2005 |
Haslbeck M, Miess A, Stromer T, Walter S, Buchner J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. Journal of Biological Chemistry. 280: 23861-23868. PMID 15843375 DOI: 10.1074/Jbc.M502697200 |
0.49 |
|
| 2004 |
Falsone SF, Leptihn S, Osterauer A, Haslbeck M, Buchner J. Oncogenic mutations reduce the stability of SRC kinase. Journal of Molecular Biology. 344: 281-291. PMID 15504417 DOI: 10.1016/J.Jmb.2004.08.091 |
0.306 |
|
| 2004 |
Feige MJ, Walter S, Buchner J. Folding mechanism of the CH2 antibody domain. Journal of Molecular Biology. 344: 107-118. PMID 15504405 DOI: 10.1016/J.Jmb.2004.09.033 |
0.467 |
|
| 2004 |
Gräwert T, Kaiser J, Zepeck F, Laupitz R, Hecht S, Amslinger S, Schramek N, Schleicher E, Weber S, Haslbeck M, Buchner J, Rieder C, Arigoni D, Bacher A, Eisenreich W, et al. IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis. Journal of the American Chemical Society. 126: 12847-55. PMID 15469281 DOI: 10.1021/Ja0471727 |
0.331 |
|
| 2004 |
Haslbeck M, Ignatiou A, Saibil H, Helmich S, Frenzl E, Stromer T, Buchner J. A Domain in the N-terminal Part of Hsp26 is Essential for Chaperone Function and Oligomerization Journal of Molecular Biology. 343: 445-455. PMID 15451672 DOI: 10.1016/J.Jmb.2004.08.048 |
0.493 |
|
| 2004 |
Richter K, Walter S, Buchner J. The Co-chaperone Sba1 Connects the ATPase Reaction of Hsp90 to the Progression of the Chaperone Cycle Journal of Molecular Biology. 342: 1403-1413. PMID 15364569 DOI: 10.1016/J.Jmb.2004.07.064 |
0.499 |
|
| 2004 |
Müller L, Schaupp A, Walerych D, Wegele H, Buchner J. Hsp90 Regulates the Activity of Wild Type p53 under Physiological and Elevated Temperatures Journal of Biological Chemistry. 279: 48846-48854. PMID 15358771 DOI: 10.1074/Jbc.M407687200 |
0.46 |
|
| 2004 |
Mayer M, Frey S, Koivunen P, Myllyharju J, Buchner J. Influence of the oxidoreductase ERp57 on the folding of an antibody Fab fragment Journal of Molecular Biology. 341: 1077-1084. PMID 15328618 DOI: 10.1016/J.Jmb.2004.06.068 |
0.459 |
|
| 2004 |
Hainzl O, Wegele H, Richter K, Buchner J. Cns1 Is an Activator of the Ssa1 ATPase Activity Journal of Biological Chemistry. 279: 23267-23273. PMID 15044454 DOI: 10.1074/Jbc.M402189200 |
0.525 |
|
| 2004 |
Mayer M, Buchner J. Refolding of inclusion body proteins. Methods in Molecular Medicine. 94: 239-254. PMID 14959834 DOI: 10.1385/1-59259-679-7:239 |
0.398 |
|
| 2004 |
Haslbeck M, Braun N, Stromer T, Richter B, Model N, Weinkauf S, Buchner J. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. The Embo Journal. 23: 638-49. PMID 14749732 DOI: 10.1038/sj.emboj.7600080 |
0.342 |
|
| 2004 |
Wegele H, Müller L, Buchner J. Hsp70 and Hsp90--a relay team for protein folding. Reviews of Physiology Biochemistry and Pharmacology. 151: 1-44. PMID 14740253 DOI: 10.1007/S10254-003-0021-1 |
0.501 |
|
| 2004 |
Vinci F, Catharino S, Frey S, Buchner J, Marino G, Pucci P, Ruoppolo M. Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase. The Journal of Biological Chemistry. 279: 15059-66. PMID 14729662 DOI: 10.1074/Jbc.M311480200 |
0.775 |
|
| 2004 |
Stromer T, Fischer E, Richter K, Haslbeck M, Buchner J. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. The Journal of Biological Chemistry. 279: 11222-8. PMID 14722093 DOI: 10.1074/Jbc.M310149200 |
0.528 |
|
| 2004 |
Grimminger V, Richter K, Imhof A, Buchner J, Walter S. The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104 Journal of Biological Chemistry. 279: 7378-7383. PMID 14668331 DOI: 10.1074/Jbc.M312403200 |
0.434 |
|
| 2004 |
Scheibel T, Buchner J. Book Review: Methods in Molecular Biology, Vol. 232: Protein Misfolding and Disease: Principles and Methods. Edited by Peter Bross and Niels Gregerson. Chembiochem. 5: 1154-1155. DOI: 10.1002/Cbic.200300144 |
0.531 |
|
| 2003 |
Dawson R, Müller L, Dehner A, Klein C, Kessler H, Buchner J. The N-terminal domain of p53 is natively unfolded Journal of Molecular Biology. 332: 1131-1141. PMID 14499615 DOI: 10.1016/J.Jmb.2003.08.008 |
0.403 |
|
| 2003 |
Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H. NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol. Chembiochem. 4: 870-877. PMID 12964162 DOI: 10.1002/Cbic.200300658 |
0.446 |
|
| 2003 |
Wegele H, Muschler P, Bunck M, Reinstein J, Buchner J. Dissection of the Contribution of Individual Domains to the ATPase Mechanism of Hsp90 Journal of Biological Chemistry. 278: 39303-39310. PMID 12890674 DOI: 10.1074/Jbc.M305751200 |
0.456 |
|
| 2003 |
Mayer M, Reinstein J, Buchner J. Modulation of the ATPase cycle of BiP by peptides and proteins. Journal of Molecular Biology. 330: 137-144. PMID 12818208 DOI: 10.1016/S0022-2836(03)00556-4 |
0.449 |
|
| 2003 |
Wegele H, Haslbeck M, Reinstein J, Buchner J. Sti1 is a novel activator of the Ssa proteins. Journal of Biological Chemistry. 278: 25970-25976. PMID 12716905 DOI: 10.1074/Jbc.M301548200 |
0.459 |
|
| 2003 |
Wegele H, Haslbeck M, Buchner J. Recombinant expression and purification of Ssa1p (Hsp70) from Saccharomyces cerevisiae using Pichia pastoris. Journal of Chromatography B. 786: 109-115. PMID 12651006 DOI: 10.1016/S1570-0232(02)00724-9 |
0.436 |
|
| 2003 |
Stromer T, Ehrnsperger M, Gaestel M, Buchner J. Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins Journal of Biological Chemistry. 278: 18015-18021. PMID 12637495 DOI: 10.1074/Jbc.M301640200 |
0.48 |
|
| 2003 |
Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase - Binding prevents the N-terminal dimerization reaction during the ATPase cycle Journal of Biological Chemistry. 278: 10328-10333. PMID 12525481 DOI: 10.1074/Jbc.M213094200 |
0.467 |
|
| 2002 |
Walter S, Buchner J. Molecular chaperones--cellular machines for protein folding. Angewandte Chemie. 41: 1098-1113. PMID 12491239 DOI: 10.1002/1521-3773(20020402)41:7<1098::Aid-Anie1098>3.0.Co;2-9 |
0.486 |
|
| 2002 |
Buchner J. Introduction: the cellular protein folding machinery. Cellular and Molecular Life Sciences. 59: 1587-1588. PMID 12475167 DOI: 10.1007/Pl00012484 |
0.444 |
|
| 2002 |
Bell S, Klein C, Müller L, Hansen S, Buchner J. p53 contains large unstructured regions in its native state. Journal of Molecular Biology. 322: 917-927. PMID 12367518 DOI: 10.1016/S0022-2836(02)00848-3 |
0.395 |
|
| 2002 |
Richter K, Reinstein J, Buchner J. N-terminal Residues Regulate the Catalytic Efficiency of the Hsp90 ATPase Cycle Journal of Biological Chemistry. 277: 44905-44910. PMID 12235160 DOI: 10.1074/Jbc.M208457200 |
0.473 |
|
| 2002 |
Thies MJW, Talamo F, Mayer M, Bell S, Ruoppolo M, Marino G, Buchner J. Folding and Oxidation of the Antibody Domain CH3 Journal of Molecular Biology. 319: 1267-1277. PMID 12079363 DOI: 10.1016/S0022-2836(02)00375-3 |
0.387 |
|
| 2002 |
Buchner J, Rudolph R, Lilie H. Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains. Journal of Molecular Biology. 318: 829-36. PMID 12054826 DOI: 10.1016/S0022-2836(02)00171-7 |
0.575 |
|
| 2002 |
Knarr G, Kies U, Bell S, Mayer M, Buchner J. Interaction of the chaperone BiP with an antibody domain: implications for the chaperone cycle. Journal of Molecular Biology. 318: 611-620. PMID 12054809 DOI: 10.1016/S0022-2836(02)00166-3 |
0.481 |
|
| 2002 |
Bell S, Hansen S, Buchner J. Refolding and structural characterization of the human p53 tumor suppressor protein. Biophysical Chemistry. 96: 243-257. PMID 12034444 DOI: 10.1016/S0301-4622(02)00011-X |
0.389 |
|
| 2002 |
Kurek I, Pirkl F, Fischer E, Buchner J, Breiman A. Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. Planta. 215: 119-26. PMID 12012248 DOI: 10.1007/S00425-001-0722-0 |
0.433 |
|
| 2002 |
Haslbeck M, Buchner J. Chaperone function of sHsps. Progress in Molecular and Subcellular Biology. 28: 37-59. PMID 11908065 DOI: 10.1007/978-3-642-56348-5_3 |
0.488 |
|
| 2002 |
Grallert H, Buchner J. Review: a structural view of the GroE chaperone cycle. Journal of Structural Biology. 135: 95-103. PMID 11580259 DOI: 10.1006/Jsbi.2001.4387 |
0.461 |
|
| 2002 |
Knarr G, Kies U, Bell S, Mayer M, Buchner J. Erratum to “Interaction of the Chaperone BiP with an Antibody Domain: Implications for the Chaperone Cycle” Journal of Molecular Biology. 323: 407. DOI: 10.1016/S0022-2836(02)01002-1 |
0.39 |
|
| 2001 |
Richter K, Buchner J. Hsp90: chaperoning signal transduction. Journal of Cellular Physiology. 188: 281-90. PMID 11473354 DOI: 10.1002/Jcp.1131 |
0.475 |
|
| 2001 |
Pirkl F, Fischer E, Modrow S, Buchner J. Localization of the chaperone domain of FKBP52. The Journal of Biological Chemistry. 276: 37034-41. PMID 11473108 DOI: 10.1074/Jbc.M102595200 |
0.461 |
|
| 2001 |
Richter K, Muschler P, Hainzl O, Buchner J. Coordinated ATP hydrolysis by the Hsp90 dimer. The Journal of Biological Chemistry. 276: 33689-96. PMID 11441008 DOI: 10.1074/Jbc.M103832200 |
0.473 |
|
| 2001 |
Thies MJ, Kammermeier R, Richter K, Buchner J. The alternatively folded state of the antibody C(H)3 domain. Journal of Molecular Biology. 309: 1077-85. PMID 11399080 DOI: 10.1006/Jmbi.2001.4707 |
0.414 |
|
| 2001 |
Pirkl F, Buchner J. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. Journal of Molecular Biology. 308: 795-806. PMID 11350175 DOI: 10.1006/Jmbi.2001.4595 |
0.455 |
|
| 2001 |
Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry. 40: 1764-1773. PMID 11327838 DOI: 10.1021/Bi001916L |
0.464 |
|
| 2001 |
Augustine JG, de La Calle A, Knarr G, Buchner J, Frederick CA. The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip. The Journal of Biological Chemistry. 276: 3287-94. PMID 11036070 DOI: 10.1074/Jbc.M005221200 |
0.406 |
|
| 2000 |
Weikl T, Muschler P, Richter K, Veit T, Reinstein J, Buchner J. C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. Journal of Molecular Biology. 303: 583-92. PMID 11054293 DOI: 10.1006/Jmbi.2000.4157 |
0.433 |
|
| 2000 |
Mayr C, Richter K, Lilie H, Buchner J. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. The Journal of Biological Chemistry. 275: 34140-6. PMID 10942767 DOI: 10.1074/Jbc.M005251200 |
0.484 |
|
| 2000 |
Ehrnsperger M, Gaestel M, Buchner J. Analysis of Chaperone Properties of Small Hsp Methods of Molecular Biology. 99: 421-429. PMID 10909096 DOI: 10.1385/1-59259-054-3:421 |
0.343 |
|
| 2000 |
Mayer M, Kies U, Kammermeier R, Buchner J. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. The Journal of Biological Chemistry. 275: 29421-5. PMID 10893409 DOI: 10.1074/Jbc.M002655200 |
0.468 |
|
| 2000 |
Grallert H, Rutkat K, Buchner J. Limits of protein folding inside GroE complexes. The Journal of Biological Chemistry. 275: 20424-30. PMID 10779510 DOI: 10.1074/Jbc.M002243200 |
0.462 |
|
| 2000 |
Lindner RA, Carver JA, Ehrnsperger M, Buchner J, Esposito G, Behlke J, Lutsch G, Kotlyarov A, Gaestel M. Mouse Hsp25, a small heat shock protein Febs Journal. 267: 1923-1932. PMID 10727931 DOI: 10.1046/J.1432-1327.2000.01188.X |
0.493 |
|
| 2000 |
Haslbeck M, Walke S, Stromer T, Ehrnsperger M, White HE, Chen S, Saibil HR, Buchner J. Hsp26: a temperature-regulated chaperone. The Embo Journal. 18: 6744-51. PMID 10581247 DOI: 10.1093/Emboj/18.23.6744 |
0.451 |
|
| 1999 |
Scheibel T, Weikl T, Rimerman R, Smith D, Lindquist S, Buchner J. Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Molecular Microbiology. 34: 701-13. PMID 10564510 DOI: 10.1046/J.1365-2958.1999.01632.X |
0.709 |
|
| 1999 |
Weikl T, Abelmann K, Buchner J. An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. Journal of Molecular Biology. 293: 685-91. PMID 10543959 DOI: 10.1006/Jmbi.1999.3172 |
0.446 |
|
| 1999 |
Knarr G, Modrow S, Todd A, Gething MJ, Buchner J. BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip. The Journal of Biological Chemistry. 274: 29850-7. PMID 10514465 DOI: 10.1074/Jbc.274.42.29850 |
0.356 |
|
| 1999 |
Thies MJ, Mayer J, Augustine JG, Frederick CA, Lilie H, Buchner J. Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization. Journal of Molecular Biology. 293: 67-79. PMID 10512716 DOI: 10.1006/Jmbi.1999.3128 |
0.405 |
|
| 1999 |
Grallert H, Buchner J. Analysis of GroE-assisted folding under nonpermissive conditions. The Journal of Biological Chemistry. 274: 20171-7. PMID 10400632 DOI: 10.1074/Jbc.274.29.20171 |
0.48 |
|
| 1999 |
Rogalla T, Ehrnsperger M, Preville X, Kotlyarov A, Lutsch G, Ducasse C, Paul C, Wieske M, Arrigo AP, Buchner J, Gaestel M. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. The Journal of Biological Chemistry. 274: 18947-56. PMID 10383393 DOI: 10.1074/Jbc.274.27.18947 |
0.367 |
|
| 1999 |
Beissinger M, Rutkat K, Buchner J. Catalysis, Commitment and Encapsulation during GroE-mediated Folding Journal of Molecular Biology. 289: 1075-1092. PMID 10369783 DOI: 10.1006/Jmbi.1999.2780 |
0.464 |
|
| 1999 |
Ehrnsperger M, Lilie H, Gaestel M, Buchner J. The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species. The Journal of Biological Chemistry. 274: 14867-74. PMID 10329686 DOI: 10.1074/Jbc.274.21.14867 |
0.455 |
|
| 1999 |
Buchner J. Hsp90 & Co. – a holding for folding Trends in Biochemical Sciences. 24: 136-141. PMID 10322418 DOI: 10.1016/S0968-0004(99)01373-0 |
0.528 |
|
| 1999 |
Scheibel T, Siegmund HI, Jaenicke R, Ganz P, Lilie H, Buchner J. The charged region of Hsp90 modulates the function of the N-terminal domain. Proceedings of the National Academy of Sciences of the United States of America. 96: 1297-302. PMID 9990018 DOI: 10.1073/Pnas.96.4.1297 |
0.701 |
|
| 1999 |
Grallert H, Rutkat K, Buchner J. GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase. The Journal of Biological Chemistry. 273: 33305-10. PMID 9837903 DOI: 10.1074/Jbc.273.50.33305 |
0.487 |
|
| 1998 |
Nichtl A, Buchner J, Jaenicke R, Rudolph R, Scheibel T. Folding and association of beta-Galactosidase. Journal of Molecular Biology. 282: 1083-91. PMID 9753555 DOI: 10.1006/Jmbi.1998.2075 |
0.714 |
|
| 1998 |
Scheibel T, Buchner J. The Hsp90 complex--a super-chaperone machine as a novel drug target. Biochemical Pharmacology. 56: 675-82. PMID 9751071 DOI: 10.1016/S0006-2952(98)00120-8 |
0.632 |
|
| 1998 |
Zavialov A, Benndorf R, Ehrnsperger M, Zav’yalov V, Dudich I, Buchner J, Gaestel M. The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25 International Journal of Biological Macromolecules. 22: 163-173. PMID 9650071 DOI: 10.1016/S0141-8130(98)00014-2 |
0.484 |
|
| 1998 |
Ehrnsperger M, Hergersberg C, Wienhues U, Nichtl A, Buchner J. Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25. Analytical Biochemistry. 259: 218-25. PMID 9618200 DOI: 10.1006/Abio.1998.2630 |
0.457 |
|
| 1998 |
Veinger L, Diamant S, Buchner J, Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network Journal of Biological Chemistry. 273: 11032-11037. PMID 9556585 DOI: 10.1074/Jbc.273.18.11032 |
0.452 |
|
| 1998 |
Buchner J, Weikl T, Bügl H, Pirkl F, Bose S. Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52. Methods in Enzymology. 290: 418-429. PMID 9534179 DOI: 10.1016/S0076-6879(98)90035-0 |
0.421 |
|
| 1998 |
Buchner J, Bose S, Mayr C, Jakob U. Purification and characterization of prokaryotic and eukaryotic Hsp90. Methods in Enzymology. 290: 409-18. PMID 9534178 DOI: 10.1016/S0076-6879(98)90034-9 |
0.502 |
|
| 1998 |
Buchner J, Ehrnsperger M, Gaestel M, Walke S. Purification And Characterization Of Small Heat Shock Proteins Methods in Enzymology. 290: 339-349. PMID 9534174 DOI: 10.1016/S0076-6879(98)90030-1 |
0.466 |
|
| 1998 |
Buchner J, Grallert H, Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods in Enzymology. 290: 323-338. PMID 9534173 DOI: 10.1016/S0076-6879(98)90029-5 |
0.477 |
|
| 1998 |
Scheibel T, Weikl T, Buchner J. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proceedings of the National Academy of Sciences of the United States of America. 95: 1495-9. PMID 9465043 DOI: 10.1073/Pnas.95.4.1495 |
0.654 |
|
| 1997 |
Scheibel T, Neuhofen S, Weikl T, Mayr C, Reinstein J, Vogel PD, Buchner J. ATP-binding properties of human Hsp90. The Journal of Biological Chemistry. 272: 18608-13. PMID 9228028 DOI: 10.1074/Jbc.272.30.18608 |
0.596 |
|
| 1997 |
Sparrer H, Buchner J. How GroES regulates binding of nonnative protein to GroEL. The Journal of Biological Chemistry. 272: 14080-6. PMID 9162032 DOI: 10.1074/Jbc.272.22.14080 |
0.425 |
|
| 1997 |
Sparrer H, Rutkat K, Buchner J. Catalysis of protein folding by symmetric chaperone complexes. Proceedings of the National Academy of Sciences of the United States of America. 94: 1096-100. PMID 9037012 DOI: 10.1073/Pnas.94.4.1096 |
0.499 |
|
| 1997 |
Ehrnsperger M, Gräber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. The Embo Journal. 16: 221-9. PMID 9029143 DOI: 10.1093/Emboj/16.2.221 |
0.482 |
|
| 1997 |
Bose S, Weikl T, Bügl H, Buchner J. Chaperone function of Hsp90-associated proteins. Science (New York, N.Y.). 274: 1715-7. PMID 8939863 DOI: 10.1126/Science.274.5293.1715 |
0.471 |
|
| 1996 |
Langer T, Buchner J, Bukau B. Chaperone function on Crete: A meeting report Cell Stress and Chaperones. 1: 5-12. PMID 9222582 DOI: 10.1379/1466-1268(1996)001<0005:Cfocam>2.3.Co;2 |
0.389 |
|
| 1996 |
Jakob U, Scheibel T, Bose S, Reinstein J, Buchner J. Assessment of the ATP binding properties of Hsp90. The Journal of Biological Chemistry. 271: 10035-41. PMID 8626558 DOI: 10.1074/Jbc.271.17.10035 |
0.613 |
|
| 1996 |
Sparrer H, Lilie H, Buchner J. Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants. Journal of Molecular Biology. 258: 74-87. PMID 8613994 DOI: 10.1006/Jmbi.1996.0235 |
0.467 |
|
| 1996 |
Buchner J. Supervising the fold: functional principles of molecular chaperones. The Faseb Journal. 10: 10-19. DOI: 10.1096/Fasebj.10.1.8566529 |
0.476 |
|
| 1995 |
Gething MJ, Blond-Elguindi S, Buchner J, Fourie A, Knarr G, Modrow S, Nanu L, Segal M, Sambrook J. Binding sites for Hsp70 molecular chaperones in natural proteins. Cold Spring Harbor Symposia On Quantitative Biology. 60: 417-28. PMID 8824415 DOI: 10.1101/Sqb.1995.060.01.046 |
0.417 |
|
| 1995 |
Jakob U, Meyer I, Bügl H, André S, Bardwell JC, Buchner J. Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. The Journal of Biological Chemistry. 270: 14412-9. PMID 7782303 DOI: 10.1074/Jbc.270.24.14412 |
0.466 |
|
| 1995 |
Bose S, Lilie H, Buchner J, Freedman RB. The in vitro catalysis of protein folding by endoplasmic reticulum luminal peptidyl prolyl cis-trans isomerase. Biochemical Society Transactions. 23: 63S. PMID 7758779 DOI: 10.1042/Bst023063S |
0.366 |
|
| 1995 |
Lilie H, Rudolph R, Buchner J. Association of antibody chains at different stages of folding: Prolyl isomerization occurs after formation of quaternary structure Journal of Molecular Biology. 248: 190-201. PMID 7731044 DOI: 10.1006/Jmbi.1995.0211 |
0.615 |
|
| 1995 |
Jakob U, Lilie H, Meyer I, Buchner J. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. The Journal of Biological Chemistry. 270: 7288-94. PMID 7706269 DOI: 10.1074/Jbc.270.13.7288 |
0.447 |
|
| 1995 |
Lilie H, Buchner J. Domain interactions stabilize the alternatively folded state of an antibody Fab fragment. Febs Letters. 362: 43-6. PMID 7698350 DOI: 10.1016/0014-5793(95)00203-L |
0.387 |
|
| 1995 |
Lilie H, Buchner J. Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding. Proceedings of the National Academy of Sciences of the United States of America. 92: 8100-4. PMID 7667251 DOI: 10.1073/Pnas.92.18.8100 |
0.482 |
|
| 1995 |
Lilie H, Jaenicke R, Buchner J. Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment. Protein Science : a Publication of the Protein Society. 4: 917-24. PMID 7663347 DOI: 10.1002/Pro.5560040511 |
0.611 |
|
| 1995 |
Viitanen PV, Schmidt M, Buchner J, Suzuki T, Vierling E, Dickson R, Lorimer GH, Gatenby A, Soll J. Functional characterization of the higher plant chloroplast chaperonins Journal of Biological Chemistry. 270: 18158-18164. PMID 7629128 DOI: 10.1074/Jbc.270.30.18158 |
0.327 |
|
| 1995 |
Knarr G, Gething MJ, Modrow S, Buchner J. BiP binding sequences in antibodies. The Journal of Biological Chemistry. 270: 27589-94. PMID 7499221 DOI: 10.1074/Jbc.270.46.27589 |
0.396 |
|
| 1994 |
Jakob U, Buchner J. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones Trends in Biochemical Sciences. 19: 205-211. PMID 7914036 DOI: 10.1016/0968-0004(94)90023-X |
0.468 |
|
| 1994 |
Schmidt M, Rutkat K, Rachel R, Pfeifer G, Jaenicke R, Viitanen P, Lorimer G, Buchner J. Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (New York, N.Y.). 265: 656-9. PMID 7913554 DOI: 10.1126/Science.7913554 |
0.582 |
|
| 1994 |
Lilie H, McLaughlin S, Freedman R, Buchner J. Influence of protein disulfide isomerase (PDI) on antibody folding in vitro. Journal of Biological Chemistry. 269: 14290-14296. DOI: 10.1016/s0021-9258(17)36787-x |
0.308 |
|
| 1994 |
Buchner J. The biology of heat shock proteins and molecular chaperones: edited by R.I. Morimoto, A. Tisslères and C. Georgopoulos, Cold Spring Harbor Laboratory Press, 1994. $97.00 (vii + 610 pages) ISBN 0 87969 427 0 Trends in Biochemical Sciences. 19: 559. DOI: 10.1016/0968-0004(94)90065-5 |
0.367 |
|
| 1994 |
Knauf U, Jakob U, Engel K, Buchner J, Gaestel M. Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance. The Embo Journal. 13: 54-60. DOI: 10.1002/J.1460-2075.1994.Tb06234.X |
0.416 |
|
| 1993 |
Theuer CP, Buchner J, FitzGerald D, Pastan I. The N-terminal region of the 37-kDa translocated fragment of Pseudomonas exotoxin A aborts translocation by promoting its own export after microsomal membrane insertion. Proceedings of the National Academy of Sciences of the United States of America. 90: 7774-8. PMID 8356083 DOI: 10.1073/Pnas.90.16.7774 |
0.321 |
|
| 1993 |
Lilie H, Lang K, Rudolph R, Buchner J. Prolyl isomerases catalyze antibody folding in vitro Protein Science. 2: 1490-1496. PMID 8104614 DOI: 10.1002/Pro.5560020913 |
0.608 |
|
| 1993 |
Wiech H, Buchner J, Zimmermann M, Zimmermann R, Jakob U. Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes. Journal of Biological Chemistry. 268: 7414-7421. DOI: 10.1016/s0021-9258(18)53190-2 |
0.322 |
|
| 1992 |
Wiech H, Buchner J, Zimmermann R, Jakob U. Hsp90 chaperones protein folding in vitro. Nature. 358: 169-170. PMID 1614549 DOI: 10.1038/358169A0 |
0.515 |
|
| 1992 |
Brinkmann U, Buchner J, Pastan I. Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections. Proceedings of the National Academy of Sciences of the United States of America. 89: 3075-9. PMID 1557415 DOI: 10.1073/Pnas.89.7.3075 |
0.434 |
|
| 1992 |
Buchner J, Brinkmann U, Pastan I. Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase. Bio/Technology (Nature Publishing Company). 10: 682-5. PMID 1369490 DOI: 10.1038/Nbt0692-682 |
0.469 |
|
| 1992 |
Kern G, Schmidt M, Buchner J, Jaenicke R. Glycosylation inhibits the interaction of invertase with the chaperone GroEL. Febs Letters. 305: 203-5. PMID 1363729 DOI: 10.1016/0014-5793(92)80667-6 |
0.587 |
|
| 1992 |
Buchner J, Pastan I, Brinkmann U. A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Analytical Biochemistry. 205: 263-70. PMID 1332541 DOI: 10.1016/0003-2697(92)90433-8 |
0.441 |
|
| 1991 |
Buchner J, Renner M, Lilie H, Hinz HJ, Jaenicke R, Kiefhabel T, Rudolph R. Alternatively folded states of an immunoglobulin. Biochemistry. 30: 6922-9. PMID 1906346 DOI: 10.1021/Bi00242A016 |
0.671 |
|
| 1991 |
Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30: 1586-91. PMID 1671555 DOI: 10.1021/Bi00220A020 |
0.802 |
|
| 1991 |
Buchner J, Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technology (Nature Publishing Company). 9: 157-62. PMID 1369317 DOI: 10.1038/Nbt0291-157 |
0.581 |
|
| 1991 |
Buchner J, Rudolph R. Routes to active proteins from transformed microorganisms. Current Opinion in Biotechnology. 2: 532-538. PMID 1367672 DOI: 10.1016/0958-1669(91)90077-I |
0.601 |
|
| 1991 |
Kiefhaber T, Rudolph R, Kohler HH, Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology (Nature Publishing Company). 9: 825-9. PMID 1367356 DOI: 10.1038/Nbt0991-825 |
0.734 |
|
| 1990 |
Buchner J, Kiefhaber T. Folding pathway enigma. Nature. 343: 601-2. PMID 2304534 DOI: 10.1038/343601B0 |
0.589 |
|
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